Analytical Data
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Gene name
HSPA1L
- Application
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Alternative Names
Heat shock 70 kDa protein 1-like; Heat shock 70 kDa protein 1-Hom; HSP70-Hom; Heat shock protein family A member 1L; HSPA1L; Homo sapiens; Human; Heat shock 70 kDa protein 1L
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Species
Human
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Source
E. coli
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Tag
Strep;His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P34931
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Expression Region
A2-D641
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Protein Length
Partial
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
HSPA1L, a member of the heat shock protein 70 (HSP70) family, plays a significant role in cellular stress response, protein folding, and degradation pathways. Its expression is particularly elevated during stressful conditions such as heat shock, oxidative stress, and inflammation, suggesting its protective role in maintaining cellular homeostasis. Research has shown that HSPA1L is involved in various biological processes, including cell proliferation, apoptosis, and differentiation, making it a crucial factor in both normal physiology and disease states. Importantly, HSPA1L has also been implicated in cancer progression, where it can modulate tumor growth and response to therapy. Given its multifunctional role, the recombinant production of HSPA1L protein is of great interest for understanding its mechanisms and for potential therapeutic applications. Studies focusing on the characterization and functional analysis of HSPA1L recombinant protein aim to provide insights into its specific interactions, regulatory pathways, and role in diseases, particularly in oncological contexts. The ability to produce HSPA1L in a recombinant form allows researchers to perform detailed biochemical assays, investigate its chaperone activity, and explore its potential as a biomarker or therapeutic target. As such, HSPA1L represents a promising avenue for research in cellular stress responses, cancer biology, and other related fields.
